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Isolation, purification and properties of Bacillus mesentericus proteinases

Koltukova, N.V.; Bondarchuk, A.A.; Zakharova, I.I.

Mikrobiolohichnyi Zhurnal 44(3): 12-15

1982

ISSN/ISBN: 0201-8462
PMID: 6750327
Document Number: 185347
Four fractions of B. mesentericus proteinases were isolated by ion exchange chromatography and isoelectrofocusing borate-polyol. Two fractions are alkaline serine-type proteases, 1 is a neutral serine protease and 1 is a neutral metal-dependent protease. The neutral fractions, by isoelectrofocusing and disc electrophoresis, are heterogeneous and contain inactive admixtures. Alkaline proteinases were purified 1.77-fold relative to proteolytic activity and 13.7-fold relative to elastase activity; corresponding purification values for the neutral proteinases were 1.03- and 4.5-fold, respectively. The composition of the proteolytic complex of B. mesentericus is similar to that the NoVo-type subtilisins.

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